SitesBLAST
Comparing AZOBR_RS19480 FitnessBrowser__azobra:AZOBR_RS19480 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
37% identity, 94% coverage: 26:545/556 of query aligns to 18:535/541 of Q5SKN9
- T184 (= T196) binding
- G302 (= G311) binding
- Q322 (≠ H331) binding
- G323 (≠ M332) binding
- T327 (= T336) binding
- E328 (= E337) binding
- D418 (= D428) binding
- K435 (= K445) binding
- K439 (≠ I449) binding
P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
35% identity, 88% coverage: 52:542/556 of query aligns to 30:495/503 of P9WQ37
- K172 (= K204) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R227) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E229) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C241) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
- A211 (≠ G243) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ Y246) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
- R244 (≠ G276) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G334) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
- W377 (= W423) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
- D382 (= D428) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
- R397 (= R443) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S450) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G452) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K534) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
34% identity, 88% coverage: 52:542/556 of query aligns to 33:495/502 of 3r44A
Sites not aligning to the query:
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
36% identity, 92% coverage: 26:536/556 of query aligns to 11:502/510 of 1v26B
- active site: T177 (= T196), H197 (≠ N216), H223 (= H240), T320 (= T336), E321 (= E337), K432 (≠ I449), W437 (≠ N454)
- binding adenosine monophosphate: G295 (= G311), S296 (≠ A312), A297 (= A313), G316 (≠ M332), Y317 (= Y333), G318 (= G334), L319 (= L335), T320 (= T336), D411 (= D428), K428 (= K445), K432 (≠ I449), W437 (≠ N454)
- binding magnesium ion: T177 (= T196), E321 (= E337)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
37% identity, 84% coverage: 26:491/556 of query aligns to 11:464/491 of 1v25A
- active site: T177 (= T196), H197 (≠ N216), H223 (= H240), T320 (= T336), E321 (= E337), K432 (≠ I449), W437 (≠ N454)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H240), V224 (≠ C241), G295 (= G311), S296 (≠ A312), A297 (= A313), Y317 (= Y333), G318 (= G334), L319 (= L335), T320 (= T336), D411 (= D428), I423 (≠ V440), K432 (≠ I449), W437 (≠ N454)
- binding magnesium ion: T177 (= T196), E321 (= E337)
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
33% identity, 87% coverage: 62:546/556 of query aligns to 50:535/538 of 6ijbB
- active site: T185 (= T196), H205 (≠ N216), H231 (= H240), S329 (≠ T336), E330 (= E337), K438 (≠ I449), W443 (≠ N454), A523 (≠ K534)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W244), G303 (= G310), A325 (≠ M332), W326 (≠ Y333), G327 (= G334), M328 (≠ L335)
- binding adenosine monophosphate: G303 (= G310), A304 (≠ G311), A305 (= A312), H324 (= H331), W326 (≠ Y333), G327 (= G334), M328 (≠ L335), S329 (≠ T336), Q359 (= Q366), D417 (= D428)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
32% identity, 87% coverage: 62:546/556 of query aligns to 50:532/533 of 6ihkB
- active site: T185 (= T196), H202 (≠ N216), H228 (= H240), S326 (≠ T336), E327 (= E337), K435 (≠ I449), W440 (≠ N454), K520 (= K534)
- binding adenosine-5'-diphosphate: H228 (= H240), G300 (= G310), A301 (≠ G311), A302 (= A312), H321 (= H331), A322 (≠ M332), W323 (≠ Y333), G324 (= G334), M325 (≠ L335), S326 (≠ T336), Q356 (= Q366), D414 (= D428), R429 (= R443), K520 (= K534)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
29% identity, 93% coverage: 30:545/556 of query aligns to 6:481/484 of 5gtdA
- active site: T151 (= T196), S171 (≠ N216), H195 (= H240), T288 (= T336), E289 (= E337)
- binding adenosine-5'-monophosphate: G263 (= G310), G264 (= G311), Y285 (= Y333), G286 (= G334), M287 (≠ L335), T288 (= T336), D366 (= D428), V378 (= V440)
- binding magnesium ion: F314 (≠ V371), S315 (≠ A372)
- binding 2-succinylbenzoate: H195 (= H240), S197 (≠ N242), A237 (≠ G282), L260 (≠ V307), G262 (≠ T309), G263 (= G310), G286 (= G334), M287 (≠ L335), S292 (≠ G340), Q293 (≠ P341)
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
29% identity, 93% coverage: 30:545/556 of query aligns to 6:481/485 of 5x8fB